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Volumn , Issue , 2013, Pages 127-146

Application of biophysics to the early developability assessment of therapeutic candidates and its application to enhance developability properties

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EID: 84896502272     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4614-4316-2_6     Document Type: Chapter
Times cited : (8)

References (71)
  • 1
    • 0031589944 scopus 로고    scopus 로고
    • Ion channels-basic science and clinical disease
    • Ackerman MJ, Clapham DE (1997) Ion channels-basic science and clinical disease. N Engl J Med 336(22):1575-1586.
    • (1997) N Engl J Med , vol.336 , Issue.22 , pp. 1575-1586
    • Ackerman, M.J.1    Clapham, D.E.2
  • 2
    • 74749088503 scopus 로고    scopus 로고
    • Spending on new drug development1
    • Adams CP, Brantner VV (2010) Spending on new drug development1. Health Econ 19(2):130-141.
    • (2010) Health Econ , vol.19 , Issue.2 , pp. 130-141
    • Adams, C.P.1    Brantner, V.V.2
  • 4
    • 0030926366 scopus 로고    scopus 로고
    • Targeted anti-cancer therapy using rituximab, a chimaeric anti-CD20 antibody (IDEC-C2B8) in the treatment of non-Hodgkin's B-cell lymphoma
    • Anderson DR, Grillo-Lopez A, Varns C, Chambers KS, Hanna N (1997) Targeted anti-cancer therapy using rituximab, a chimaeric anti-CD20 antibody (IDEC-C2B8) in the treatment of non-Hodgkin's B-cell lymphoma. Biochem Soc Trans 25(2):705-708.
    • (1997) Biochem Soc Trans , vol.25 , Issue.2 , pp. 705-708
    • Anderson, D.R.1    Grillo-Lopez, A.2    Varns, C.3    Chambers, K.S.4    Hanna, N.5
  • 5
    • 34848814457 scopus 로고    scopus 로고
    • A high-throughput method for detection of protein selfassociation and second virial coefficient using size-exclusion chromatography through simultaneous measurement of concentration and scattered light intensity
    • Bajaj H, Sharma VK, Kalonia DS (2007) A high-throughput method for detection of protein selfassociation and second virial coefficient using size-exclusion chromatography through simultaneous measurement of concentration and scattered light intensity. Pharm Res 24(11):2071-2083.
    • (2007) Pharm Res , vol.24 , Issue.11 , pp. 2071-2083
    • Bajaj, H.1    Sharma, V.K.2    Kalonia, D.S.3
  • 6
    • 0032100706 scopus 로고    scopus 로고
    • Affinity dependence of the B cell response to antigen: a threshold, a ceiling, and the importance of off-rate
    • Batista FD, Neuberger MS (1998) Affinity dependence of the B cell response to antigen: a threshold, a ceiling, and the importance of off-rate. Immunity 8(6):751-759.
    • (1998) Immunity , vol.8 , Issue.6 , pp. 751-759
    • Batista, F.D.1    Neuberger, M.S.2
  • 8
    • 80052263787 scopus 로고    scopus 로고
    • The effects of shear flow on protein structure and function
    • Bekard IB, Asimakis P, Bertolini J, Dunstan DE (2011) The effects of shear flow on protein structure and function. Biopolymers 95(11):733-745.
    • (2011) Biopolymers , vol.95 , Issue.11 , pp. 733-745
    • Bekard, I.B.1    Asimakis, P.2    Bertolini, J.3    Dunstan, D.E.4
  • 9
    • 35348827271 scopus 로고    scopus 로고
    • Determining antibody stability: creation of solid-liquid interfacial effects within a high shear environment
    • Biddlecombe JG, Craig AV, Zhang H, Uddin S, Mulot S, Fish BC, Bracewell DG (2007) Determining antibody stability: creation of solid-liquid interfacial effects within a high shear environment. Biotechnol Prog 23(5):1218-1222.
    • (2007) Biotechnol Prog , vol.23 , Issue.5 , pp. 1218-1222
    • Biddlecombe, J.G.1    Craig, A.V.2    Zhang, H.3    Uddin, S.4    Mulot, S.5    Fish, B.C.6    Bracewell, D.G.7
  • 10
    • 0034718615 scopus 로고    scopus 로고
    • Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity
    • Boder ET, Midelfort KS, Wittrup KD (2000) Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity. Proc Natl Acad Sci USA 97(20):10701-10705.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.20 , pp. 10701-10705
    • Boder, E.T.1    Midelfort, K.S.2    Wittrup, K.D.3
  • 11
    • 79955666020 scopus 로고    scopus 로고
    • Introduction to current and future protein therapeutics: a protein engineering perspective
    • Carter PJ (2011) Introduction to current and future protein therapeutics: a protein engineering perspective. Exp Cell Res 317(9):1261-1269.
    • (2011) Exp Cell Res , vol.317 , Issue.9 , pp. 1261-1269
    • Carter, P.J.1
  • 13
    • 77951529848 scopus 로고    scopus 로고
    • Therapeutic antibodies for autoimmunity and inflammation
    • Chan AC, Carter PJ (2010) Therapeutic antibodies for autoimmunity and inflammation. Nat Rev Immunol 10(5):301-316.
    • (2010) Nat Rev Immunol , vol.10 , Issue.5 , pp. 301-316
    • Chan, A.C.1    Carter, P.J.2
  • 14
    • 70449112652 scopus 로고    scopus 로고
    • Long- and short-range electrostatic interactions affect the rheology of highly concentrated antibody solutions
    • Chari R, Jerath K, Badkar AV, Kalonia DS (2009) Long- and short-range electrostatic interactions affect the rheology of highly concentrated antibody solutions. Pharm Res 26(12):2607-2618.
    • (2009) Pharm Res , vol.26 , Issue.12 , pp. 2607-2618
    • Chari, R.1    Jerath, K.2    Badkar, A.V.3    Kalonia, D.S.4
  • 17
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation
    • Chi EY, Krishnan S, Randolph TW, Carpenter JF (2003a) Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation. Pharm Res 20(9):1325-1336.
    • (2003) Pharm Res , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 18
    • 0242515822 scopus 로고    scopus 로고
    • Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor
    • Chi EY, Krishnan S, Kendrick BS, Chang BS, Carpenter JF, Randolph TW (2003b) Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Protein Sci 12(5):903-913.
    • (2003) Protein Sci , vol.12 , Issue.5 , pp. 903-913
    • Chi, E.Y.1    Krishnan, S.2    Kendrick, B.S.3    Chang, B.S.4    Carpenter, J.F.5    Randolph, T.W.6
  • 19
    • 33745823893 scopus 로고    scopus 로고
    • Modulation of the effector functions of a human IgG1 through engineering of its hinge region
    • Dall'Acqua WF, Cook KE, Damschroder MM, Woods RM, Wu H (2006a) Modulation of the effector functions of a human IgG1 through engineering of its hinge region. J Immunol 177(2):1129-1138.
    • (2006) J Immunol , vol.177 , Issue.2 , pp. 1129-1138
    • Dall'Acqua, W.F.1    Cook, K.E.2    Damschroder, M.M.3    Woods, R.M.4    Wu, H.5
  • 20
    • 33747631571 scopus 로고    scopus 로고
    • Properties of human IgG1s engineered for enhanced binding to the neonatal Fc receptor (FcRn)
    • Dall'Acqua WF, Kiener PA, Wu H (2006b) Properties of human IgG1s engineered for enhanced binding to the neonatal Fc receptor (FcRn). J Biol Chem 281(33):23514-23524.
    • (2006) J Biol Chem , vol.281 , Issue.33 , pp. 23514-23524
    • Dall'Acqua, W.F.1    Kiener, P.A.2    Wu, H.3
  • 21
    • 34548324706 scopus 로고    scopus 로고
    • The cost of biopharmaceutical R&D: is biotech different?
    • DiMasi JA, Grabowski HG (2007) The cost of biopharmaceutical R&D: is biotech different? Manag Decis Econ 28(4-5):469-479.
    • (2007) Manag Decis Econ , vol.28 , Issue.4-5 , pp. 469-479
    • DiMasi, J.A.1    Grabowski, H.G.2
  • 22
    • 39049173446 scopus 로고    scopus 로고
    • Thermodynamically stable aggregation-resistant antibody domains through directed evolution
    • Famm K, Hansen L, Christ D, Winter G (2008) Thermodynamically stable aggregation-resistant antibody domains through directed evolution. J Mol Biol 376(4):926-931.
    • (2008) J Mol Biol , vol.376 , Issue.4 , pp. 926-931
    • Famm, K.1    Hansen, L.2    Christ, D.3    Winter, G.4
  • 24
    • 0029653368 scopus 로고
    • Kinetic and affinity limits on antibodies produced during immune responses
    • Foote J, Eisen HN (1995) Kinetic and affinity limits on antibodies produced during immune responses. Proc Natl Acad Sci USA 92(5):1254-1256.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.5 , pp. 1254-1256
    • Foote, J.1    Eisen, H.N.2
  • 25
    • 22544466953 scopus 로고    scopus 로고
    • Rational design of aggregationresistant bioactive peptides: reengineering human calcitonin
    • Fowler SB, Poon S, Muff R, Chiti F, Dobson CM, Zurdo J (2005) Rational design of aggregationresistant bioactive peptides: reengineering human calcitonin. Proc Natl Acad Sci USA 102(29):10105-10110.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.29 , pp. 10105-10110
    • Fowler, S.B.1    Poon, S.2    Muff, R.3    Chiti, F.4    Dobson, C.M.5    Zurdo, J.6
  • 26
    • 67649872364 scopus 로고    scopus 로고
    • Engineered protein scaffolds as next-generation antibody therapeutics
    • Gebauer M, Skerra A (2009) Engineered protein scaffolds as next-generation antibody therapeutics. Curr Opin Chem Biol 13(3):245-255.
    • (2009) Curr Opin Chem Biol , vol.13 , Issue.3 , pp. 245-255
    • Gebauer, M.1    Skerra, A.2
  • 27
    • 0001279457 scopus 로고
    • Predicting protein crystallization from a dilute solution property
    • George A, Wilson WW (1994) Predicting protein crystallization from a dilute solution property. Acta Crystallogr D Biol Crystallogr 50(Pt 4):361-365.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 361-365
    • George, A.1    Wilson, W.W.2
  • 28
    • 79951895571 scopus 로고    scopus 로고
    • Formulation development of therapeutic monoclonal antibodies using high-throughput fluorescence and static light scattering techniques:role of conformational and colloidal stability
    • Goldberg DS, Bishop SM, Shah AU, Sathish HA (2011) Formulation development of therapeutic monoclonal antibodies using high-throughput fluorescence and static light scattering techniques:role of conformational and colloidal stability. J Pharm Sci 100:1306-1315.
    • (2011) J Pharm Sci , vol.100 , pp. 1306-1315
    • Goldberg, D.S.1    Bishop, S.M.2    Shah, A.U.3    Sathish, H.A.4
  • 30
    • 77649185864 scopus 로고    scopus 로고
    • High-throughput dynamic light scattering method for measuring viscosity of concentrated protein solutions
    • He F, Becker GW, Litowski JR, Narhi LO, Brems DN, Razinkov VI (2010) High-throughput dynamic light scattering method for measuring viscosity of concentrated protein solutions. Anal Biochem 399(1):141-143.
    • (2010) Anal Biochem , vol.399 , Issue.1 , pp. 141-143
    • He, F.1    Becker, G.W.2    Litowski, J.R.3    Narhi, L.O.4    Brems, D.N.5    Razinkov, V.I.6
  • 31
    • 79955665534 scopus 로고    scopus 로고
    • Engineering the variable region of therapeutic IgG antibodies
    • Igawa T, Tsunoda H, Kuramochi T, Sampei Z, Ishii S, Hattori K (2011) Engineering the variable region of therapeutic IgG antibodies. MAbs 3(3):243-252.
    • (2011) MAbs , vol.3 , Issue.3 , pp. 243-252
    • Igawa, T.1    Tsunoda, H.2    Kuramochi, T.3    Sampei, Z.4    Ishii, S.5    Hattori, K.6
  • 32
    • 4444302074 scopus 로고    scopus 로고
    • Aggregation-resistant domain antibodies selected on phage by heat denaturation
    • Jespers L, Schon O, Famm K, Winter G (2004) Aggregation-resistant domain antibodies selected on phage by heat denaturation. Nat Biotechnol 22(9):1161-1165.
    • (2004) Nat Biotechnol , vol.22 , Issue.9 , pp. 1161-1165
    • Jespers, L.1    Schon, O.2    Famm, K.3    Winter, G.4
  • 33
    • 58549106756 scopus 로고    scopus 로고
    • High-throughput self-interaction chromatography:applications in protein formulation prediction
    • Johnson DH, Parupudi A, Wilson WW, DeLucas LJ (2009) High-throughput self-interaction chromatography:applications in protein formulation prediction. Pharm Res 26(2):296-305.
    • (2009) Pharm Res , vol.26 , Issue.2 , pp. 296-305
    • Johnson, D.H.1    Parupudi, A.2    Wilson, W.W.3    DeLucas, L.J.4
  • 34
    • 21844472999 scopus 로고    scopus 로고
    • Reduction of irreversible protein adsorption on solid surfaces by protein engineering for increased stability
    • Karlsson M, Ekeroth J, Elwing H, Carlsson U (2005) Reduction of irreversible protein adsorption on solid surfaces by protein engineering for increased stability. J Biol Chem 280(27):25558-25564.
    • (2005) J Biol Chem , vol.280 , Issue.27 , pp. 25558-25564
    • Karlsson, M.1    Ekeroth, J.2    Elwing, H.3    Carlsson, U.4
  • 35
    • 78651275679 scopus 로고    scopus 로고
    • Glycosylation influences on the aggregation propensity of therapeutic monoclonal antibodies
    • Kayser V, Chennamsetty N, Voynov V, Forrer K, Helk B, Trout BL (2011) Glycosylation influences on the aggregation propensity of therapeutic monoclonal antibodies. Biotechnol J 6(1):38-44.
    • (2011) Biotechnol J , vol.6 , Issue.1 , pp. 38-44
    • Kayser, V.1    Chennamsetty, N.2    Voynov, V.3    Forrer, K.4    Helk, B.5    Trout, B.L.6
  • 36
    • 4344645978 scopus 로고    scopus 로고
    • Can the pharmaceutical industry reduce attrition rates?
    • Kola I, Landis J (2004) Can the pharmaceutical industry reduce attrition rates? Nat Rev Drug Discov 3(8):711-715.
    • (2004) Nat Rev Drug Discov , vol.3 , Issue.8 , pp. 711-715
    • Kola, I.1    Landis, J.2
  • 37
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • Krapp S, Mimura Y, Jefferis R, Huber R, Sondermann P (2003) Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J Mol Biol 325(5):979-989.
    • (2003) J Mol Biol , vol.325 , Issue.5 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 38
    • 70149086034 scopus 로고    scopus 로고
    • Engineered therapeutic antibodies with improved effector functions
    • Kubota T, Niwa R, Satoh M, Akinaga S, Shitara K, Hanai N (2009) Engineered therapeutic antibodies with improved effector functions. Cancer Sci 100(9):1566-1572.
    • (2009) Cancer Sci , vol.100 , Issue.9 , pp. 1566-1572
    • Kubota, T.1    Niwa, R.2    Satoh, M.3    Akinaga, S.4    Shitara, K.5    Hanai, N.6
  • 39
    • 82255192512 scopus 로고    scopus 로고
    • Developability index: a rapid in silico tool for the screening of antibody aggregation propensity
    • Lauer TM, Agrawal NJ, Chennamsetty N, Egodage K, Helk B, Trout BL (2012) Developability index: a rapid in silico tool for the screening of antibody aggregation propensity. J Pharm Sci 101(1):102-115.
    • (2012) J Pharm Sci , vol.101 , Issue.1 , pp. 102-115
    • Lauer, T.M.1    Agrawal, N.J.2    Chennamsetty, N.3    Egodage, K.4    Helk, B.5    Trout, B.L.6
  • 40
    • 77951652786 scopus 로고    scopus 로고
    • A critical evaluation of self- interaction chromatography as a predictive tool for the assessment of protein-protein interactions in protein formulation development: a case study of a therapeutic monoclonal antibody
    • Le Brun V, Friess W, Bassarab S, Muhlau S, Garidel P (2010) A critical evaluation of self- interaction chromatography as a predictive tool for the assessment of protein-protein interactions in protein formulation development: a case study of a therapeutic monoclonal antibody. Eur J Pharm Biopharm 75(1):16-25.
    • (2010) Eur J Pharm Biopharm , vol.75 , Issue.1 , pp. 16-25
    • Le Brun, V.1    Friess, W.2    Bassarab, S.3    Muhlau, S.4    Garidel, P.5
  • 41
    • 27644477360 scopus 로고    scopus 로고
    • Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution
    • Liu J, Nguyen MD, Andya JD, Shire SJ (2005) Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution. J Pharm Sci 94(9):1928-1940.
    • (2005) J Pharm Sci , vol.94 , Issue.9 , pp. 1928-1940
    • Liu, J.1    Nguyen, M.D.2    Andya, J.D.3    Shire, S.J.4
  • 42
    • 12344250438 scopus 로고    scopus 로고
    • Structural genomics of GPCRs
    • Lundstrom K (2005) Structural genomics of GPCRs. Trends Biotechnol 23(2):103-108.
    • (2005) Trends Biotechnol , vol.23 , Issue.2 , pp. 103-108
    • Lundstrom, K.1
  • 43
  • 44
    • 84856561419 scopus 로고    scopus 로고
    • Correlation of second virial coefficient with solubility for proteins in salt solutions
    • Mehta CM, White ET, Litster JD (2012) Correlation of second virial coefficient with solubility for proteins in salt solutions. Biotechnol Prog 28(1):163-170.
    • (2012) Biotechnol Prog , vol.28 , Issue.1 , pp. 163-170
    • Mehta, C.M.1    White, E.T.2    Litster, J.D.3
  • 45
    • 0035081693 scopus 로고    scopus 로고
    • The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms
    • Mimura Y, Church S, Ghirlando R, Ashton PR, Dong S, Goodall M, Lund J, Jefferis R (2000) The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms. Mol Immunol 37(12-13):697-706.
    • (2000) Mol Immunol , vol.37 , Issue.12-13 , pp. 697-706
    • Mimura, Y.1    Church, S.2    Ghirlando, R.3    Ashton, P.R.4    Dong, S.5    Goodall, M.6    Lund, J.7    Jefferis, R.8
  • 46
    • 25444487734 scopus 로고    scopus 로고
    • Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observations
    • Minton AP (2005) Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observations. J Pharm Sci 94(8):1668-1675.
    • (2005) J Pharm Sci , vol.94 , Issue.8 , pp. 1668-1675
    • Minton, A.P.1
  • 47
    • 77952561651 scopus 로고    scopus 로고
    • Extracellular ion channel inhibitor antibodies
    • Naylor J, Beech DJ (2009) Extracellular ion channel inhibitor antibodies. Open Drug Discov J 1:36-42.
    • (2009) Open Drug Discov J , vol.1 , pp. 36-42
    • Naylor, J.1    Beech, D.J.2
  • 48
    • 77957361348 scopus 로고    scopus 로고
    • Development trends for human monoclonal antibody therapeutics
    • Nelson AL, Dhimolea E, Reichert JM (2010) Development trends for human monoclonal antibody therapeutics. Nat Rev Drug Discov 9(10):767-774.
    • (2010) Nat Rev Drug Discov , vol.9 , Issue.10 , pp. 767-774
    • Nelson, A.L.1    Dhimolea, E.2    Reichert, J.M.3
  • 49
    • 0022781496 scopus 로고
    • Adsorption of proteins from solution at the solid-liquid interface
    • Norde W (1986) Adsorption of proteins from solution at the solid-liquid interface. Adv Colloid Interface Sci 25(4):267-340.
    • (1986) Adv Colloid Interface Sci , vol.25 , Issue.4 , pp. 267-340
    • Norde, W.1
  • 50
    • 39149106011 scopus 로고    scopus 로고
    • Structural characterization of a mutated, ADCC-enhanced human Fc fragment
    • Oganesyan V, Damschroder MM, Leach W, Wu H, Dall'Acqua WF (2008) Structural characterization of a mutated, ADCC-enhanced human Fc fragment. Mol Immunol 45(7):1872-1882.
    • (2008) Mol Immunol , vol.45 , Issue.7 , pp. 1872-1882
    • Oganesyan, V.1    Damschroder, M.M.2    Leach, W.3    Wu, H.4    Dall'Acqua, W.F.5
  • 54
    • 48549105161 scopus 로고    scopus 로고
    • Molecular engineering and design of therapeutic antibodies
    • Presta LG (2008) Molecular engineering and design of therapeutic antibodies. Curr Opin Immunol 20(4):460-470.
    • (2008) Curr Opin Immunol , vol.20 , Issue.4 , pp. 460-470
    • Presta, L.G.1
  • 55
    • 14444277713 scopus 로고    scopus 로고
    • Interleukin-1 receptor (IL-1R) liquid formulation development using differential scanning calorimetry
    • Remmele RL Jr, Nightlinger NS, Srinivasan S, Gombotz WR (1998) Interleukin-1 receptor (IL-1R) liquid formulation development using differential scanning calorimetry. Pharm Res 15(2):200-208.
    • (1998) Pharm Res , vol.15 , Issue.2 , pp. 200-208
    • Remmele, R.L.1    Nightlinger, N.S.2    Srinivasan, S.3    Gombotz, W.R.4
  • 56
  • 57
    • 44449108578 scopus 로고    scopus 로고
    • Nature and consequences of protein-protein interactions in high protein concentration solutions
    • Saluja A, Kalonia DS (2008) Nature and consequences of protein-protein interactions in high protein concentration solutions. Int J Pharm 358(1-2):1-15.
    • (2008) Int J Pharm , vol.358 , Issue.1-2 , pp. 1-15
    • Saluja, A.1    Kalonia, D.S.2
  • 58
    • 77957843464 scopus 로고    scopus 로고
    • Intermolecular interactions of IgG1 monoclonal antibodies at high concentrations characterized by light scattering
    • Scherer TM, Liu J, Shire SJ, Minton AP (2010) Intermolecular interactions of IgG1 monoclonal antibodies at high concentrations characterized by light scattering. J Phys Chem B 114(40):12948-12957.
    • (2010) J Phys Chem B , vol.114 , Issue.40 , pp. 12948-12957
    • Scherer, T.M.1    Liu, J.2    Shire, S.J.3    Minton, A.P.4
  • 59
    • 21244462685 scopus 로고    scopus 로고
    • Protein structural perturbation and aggregation on homogeneous surfaces
    • Sethuraman A, Belfort G (2005) Protein structural perturbation and aggregation on homogeneous surfaces. Biophys J 88(2):1322-1333.
    • (2005) Biophys J , vol.88 , Issue.2 , pp. 1322-1333
    • Sethuraman, A.1    Belfort, G.2
  • 60
    • 67749109890 scopus 로고    scopus 로고
    • Effect of protein structure on deamidation rate in the Fc fragment of an IgG1 monoclonal antibody
    • Sinha S, Zhang L, Duan S, Williams TD, Vlasak J, Ionescu R, Topp EM (2009) Effect of protein structure on deamidation rate in the Fc fragment of an IgG1 monoclonal antibody. Protein Sci 18(8):1573-1584.
    • (2009) Protein Sci , vol.18 , Issue.8 , pp. 1573-1584
    • Sinha, S.1    Zhang, L.2    Duan, S.3    Williams, T.D.4    Vlasak, J.5    Ionescu, R.6    Topp, E.M.7
  • 63
    • 80053564368 scopus 로고    scopus 로고
    • Interparticle interactions in concentrated suspensions and their bulk (rheological) properties
    • Tadros T (2011) Interparticle interactions in concentrated suspensions and their bulk (rheological) properties. Adv Colloid Interface Sci 168(1-2):263-277.
    • (2011) Adv Colloid Interface Sci , vol.168 , Issue.1-2 , pp. 263-277
    • Tadros, T.1
  • 64
    • 41449114608 scopus 로고    scopus 로고
    • Self-interaction nanoparticle spectroscopy: a nanoparticle-based protein interaction assay
    • Tessier PM, Jinkoji J, Cheng YC, Prentice JL, Lenhoff AM (2008) Self-interaction nanoparticle spectroscopy: a nanoparticle-based protein interaction assay. J Am Chem Soc 130(10):3106-3112.
    • (2008) J Am Chem Soc , vol.130 , Issue.10 , pp. 3106-3112
    • Tessier, P.M.1    Jinkoji, J.2    Cheng, Y.C.3    Prentice, J.L.4    Lenhoff, A.M.5
  • 65
    • 79951768234 scopus 로고    scopus 로고
    • Effects of shear on proteins in solution
    • Thomas CR, Geer D (2011) Effects of shear on proteins in solution. Biotechnol Lett 33(3):443-456.
    • (2011) Biotechnol Lett , vol.33 , Issue.3 , pp. 443-456
    • Thomas, C.R.1    Geer, D.2
  • 66
    • 31344474356 scopus 로고    scopus 로고
    • Colloidal behavior of proteins:effects of the second virial coefficient on solubility, crystallization and aggregation of proteins in aqueous solution
    • Valente JJ, Payne RW, Manning MC, Wilson WW, Henry CS (2005) Colloidal behavior of proteins:effects of the second virial coefficient on solubility, crystallization and aggregation of proteins in aqueous solution. Curr Pharm Biotechnol 6(6):427-436.
    • (2005) Curr Pharm Biotechnol , vol.6 , Issue.6 , pp. 427-436
    • Valente, J.J.1    Payne, R.W.2    Manning, M.C.3    Wilson, W.W.4    Henry, C.S.5
  • 67
    • 79955656236 scopus 로고    scopus 로고
    • Fragmentation of monoclonal antibodies
    • Vlasak J, Ionescu R (2011) Fragmentation of monoclonal antibodies. MAbs 3(3):253-263.
    • (2011) MAbs , vol.3 , Issue.3 , pp. 253-263
    • Vlasak, J.1    Ionescu, R.2
  • 68
    • 4644335636 scopus 로고    scopus 로고
    • Reduced protein adsorption at solid interfaces by sugar excipients
    • Wendorf JR, Radke CJ, Blanch HW (2004) Reduced protein adsorption at solid interfaces by sugar excipients. Biotechnol Bioeng 87(5):565-573.
    • (2004) Biotechnol Bioeng , vol.87 , Issue.5 , pp. 565-573
    • Wendorf, J.R.1    Radke, C.J.2    Blanch, H.W.3
  • 69
    • 0642373290 scopus 로고    scopus 로고
    • Two immunoglobulin G fragment C receptor polymorphisms independently predict response to rituximab in patients with follicular lymphoma
    • Weng WK, Levy R (2003) Two immunoglobulin G fragment C receptor polymorphisms independently predict response to rituximab in patients with follicular lymphoma. J Clin Oncol 21(21):3940-3947.
    • (2003) J Clin Oncol , vol.21 , Issue.21 , pp. 3940-3947
    • Weng, W.K.1    Levy, R.2
  • 70
    • 79952453101 scopus 로고    scopus 로고
    • Use of dynamic light scattering to determine second virial coefficient in a semidilute concentration regime
    • Yadav S, Scherer TM, Shire SJ, Kalonia DS (2011) Use of dynamic light scattering to determine second virial coefficient in a semidilute concentration regime. Anal Biochem 411(2):292-296.
    • (2011) Anal Biochem , vol.411 , Issue.2 , pp. 292-296
    • Yadav, S.1    Scherer, T.M.2    Shire, S.J.3    Kalonia, D.S.4
  • 71
    • 84855891967 scopus 로고    scopus 로고
    • Viscosity behavior of high-concentration monoclonal antibody solutions: correlation with interaction parameter and electroviscous effects
    • Yadav S, Shire SJ, Kalonia DS (2012) Viscosity behavior of high-concentration monoclonal antibody solutions: correlation with interaction parameter and electroviscous effects. J Pharm Sci 101(3):998-1011.
    • (2012) J Pharm Sci , vol.101 , Issue.3 , pp. 998-1011
    • Yadav, S.1    Shire, S.J.2    Kalonia, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.